Skip to main content
NCBI home page
RNA logoLink to RNA
. 1998 May;4(5):551–565. doi: 10.1017/s1355838298980335

Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomyces cerevisiae pre-mRNA splicing factor SF1.

J C Rain 1, Z Rafi 1, Z Rhani 1, P Legrain 1, A Krämer 1
PMCID: PMC1369639  PMID: 9582097

Abstract

The modular structure of splicing factor SF1 is conserved from yeast to man and SF1 acts at early stages of spliceosome assembly in both organisms. The hnRNP K homology (KH) domain of human (h) SF1 is the major determinant for RNA binding and is essential for the activity of hSF1 in spliceosome assembly, supporting the view that binding of SF1 to RNA is essential for its function. Sequences N-terminal to the KH domain mediate the interaction between hSF1 and U2AF65, which binds to the polypyrimidine tract upstream of the 3' splice site. Moreover, yeast (y) SF1 interacts with Mud2p, the presumptive U2AF65 homologue in yeast, and the interaction domain is conserved in ySF1. The C-terminal degenerate RRMs in U2AF65 and Mud2p mediate the association with hSF1 and ySF1, respectively. Analysis of chimeric constructs of hSF1 and ySF indicates that the KH domain may serve a similar function in both systems, whereas sequences C-terminal to the KH domain are not exchangeable. Thus, these results argue for hSF1 and ySF1, as well as U2AF65 and Mud2p, being functional homologues.

Full Text

The Full Text of this article is available as a PDF (852.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abovich N., Liao X. C., Rosbash M. The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition. Genes Dev. 1994 Apr 1;8(7):843–854. doi: 10.1101/gad.8.7.843. [DOI] [PubMed] [Google Scholar]
  2. Abovich N., Rosbash M. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell. 1997 May 2;89(3):403–412. doi: 10.1016/s0092-8674(00)80221-4. [DOI] [PubMed] [Google Scholar]
  3. Adams M. D., Tarng R. S., Rio D. C. The alternative splicing factor PSI regulates P-element third intron splicing in vivo. Genes Dev. 1997 Jan 1;11(1):129–138. doi: 10.1101/gad.11.1.129. [DOI] [PubMed] [Google Scholar]
  4. Arning S., Grüter P., Bilbe G., Krämer A. Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA. RNA. 1996 Aug;2(8):794–810. [PMC free article] [PubMed] [Google Scholar]
  5. Ashley C. T., Jr, Wilkinson K. D., Reines D., Warren S. T. FMR1 protein: conserved RNP family domains and selective RNA binding. Science. 1993 Oct 22;262(5133):563–566. doi: 10.1126/science.7692601. [DOI] [PubMed] [Google Scholar]
  6. Bedford M. T., Chan D. C., Leder P. FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands. EMBO J. 1997 May 1;16(9):2376–2383. doi: 10.1093/emboj/16.9.2376. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bennett M., Michaud S., Kingston J., Reed R. Protein components specifically associated with prespliceosome and spliceosome complexes. Genes Dev. 1992 Oct;6(10):1986–2000. doi: 10.1101/gad.6.10.1986. [DOI] [PubMed] [Google Scholar]
  8. Berglund J. A., Chua K., Abovich N., Reed R., Rosbash M. The splicing factor BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC. Cell. 1997 May 30;89(5):781–787. doi: 10.1016/s0092-8674(00)80261-5. [DOI] [PubMed] [Google Scholar]
  9. Birney E., Kumar S., Krainer A. R. Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 1993 Dec 25;21(25):5803–5816. doi: 10.1093/nar/21.25.5803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Brosi R., Gröning K., Behrens S. E., Lührmann R., Krämer A. Interaction of mammalian splicing factor SF3a with U2 snRNP and relation of its 60-kD subunit to yeast PRP9. Science. 1993 Oct 1;262(5130):102–105. doi: 10.1126/science.8211112. [DOI] [PubMed] [Google Scholar]
  11. Caslini C., Spinelli O., Cazzaniga G., Golay J., De Gioia L., Pedretti A., Breviario F., Amaru R., Barbui T., Biondi A. Identification of two novel isoforms of the ZNF162 gene: a growing family of signal transduction and activator of RNA proteins. Genomics. 1997 Jun 1;42(2):268–277. doi: 10.1006/geno.1997.4705. [DOI] [PubMed] [Google Scholar]
  12. Cavaloc Y., Popielarz M., Fuchs J. P., Gattoni R., Stévenin J. Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family. EMBO J. 1994 Jun 1;13(11):2639–2649. doi: 10.1002/j.1460-2075.1994.tb06554.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Champion-Arnaud P., Gozani O., Palandjian L., Reed R. Accumulation of a novel spliceosomal complex on pre-mRNAs containing branch site mutations. Mol Cell Biol. 1995 Oct;15(10):5750–5756. doi: 10.1128/mcb.15.10.5750. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Chen T., Damaj B. B., Herrera C., Lasko P., Richard S. Self-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domain. Mol Cell Biol. 1997 Oct;17(10):5707–5718. doi: 10.1128/mcb.17.10.5707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Chiara M. D., Gozani O., Bennett M., Champion-Arnaud P., Palandjian L., Reed R. Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly. Mol Cell Biol. 1996 Jul;16(7):3317–3326. doi: 10.1128/mcb.16.7.3317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Cohen C., Parry D. A. Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins. 1990;7(1):1–15. doi: 10.1002/prot.340070102. [DOI] [PubMed] [Google Scholar]
  17. Darlix J. L., Lapadat-Tapolsky M., de Rocquigny H., Roques B. P. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses. J Mol Biol. 1995 Dec 8;254(4):523–537. doi: 10.1006/jmbi.1995.0635. [DOI] [PubMed] [Google Scholar]
  18. De Boulle K., Verkerk A. J., Reyniers E., Vits L., Hendrickx J., Van Roy B., Van den Bos F., de Graaff E., Oostra B. A., Willems P. J. A point mutation in the FMR-1 gene associated with fragile X mental retardation. Nat Genet. 1993 Jan;3(1):31–35. doi: 10.1038/ng0193-31. [DOI] [PubMed] [Google Scholar]
  19. Dignam J. D., Lebovitz R. M., Roeder R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 1983 Mar 11;11(5):1475–1489. doi: 10.1093/nar/11.5.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Draper B. W., Mello C. C., Bowerman B., Hardin J., Priess J. R. MEX-3 is a KH domain protein that regulates blastomere identity in early C. elegans embryos. Cell. 1996 Oct 18;87(2):205–216. doi: 10.1016/s0092-8674(00)81339-2. [DOI] [PubMed] [Google Scholar]
  21. Fleckner J., Zhang M., Valcárcel J., Green M. R. U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction. Genes Dev. 1997 Jul 15;11(14):1864–1872. doi: 10.1101/gad.11.14.1864. [DOI] [PubMed] [Google Scholar]
  22. Frank D., Guthrie C. An essential splicing factor, SLU7, mediates 3' splice site choice in yeast. Genes Dev. 1992 Nov;6(11):2112–2124. doi: 10.1101/gad.6.11.2112. [DOI] [PubMed] [Google Scholar]
  23. Fromont-Racine M., Rain J. C., Legrain P. Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat Genet. 1997 Jul;16(3):277–282. doi: 10.1038/ng0797-277. [DOI] [PubMed] [Google Scholar]
  24. Fu X. D. The superfamily of arginine/serine-rich splicing factors. RNA. 1995 Sep;1(7):663–680. [PMC free article] [PubMed] [Google Scholar]
  25. Gaur R. K., Valcárcel J., Green M. R. Sequential recognition of the pre-mRNA branch point by U2AF65 and a novel spliceosome-associated 28-kDa protein. RNA. 1995 Jun;1(4):407–417. [PMC free article] [PubMed] [Google Scholar]
  26. Hodges P. E., Beggs J. D. RNA splicing. U2 fulfils a commitment. Curr Biol. 1994 Mar 1;4(3):264–267. doi: 10.1016/s0960-9822(00)00061-0. [DOI] [PubMed] [Google Scholar]
  27. Igel H., Wells S., Perriman R., Ares M., Jr Conservation of structure and subunit interactions in yeast homologues of splicing factor 3b (SF3b) subunits. RNA. 1998 Jan;4(1):1–10. [PMC free article] [PubMed] [Google Scholar]
  28. Jamison S. F., Crow A., Garcia-Blanco M. A. The spliceosome assembly pathway in mammalian extracts. Mol Cell Biol. 1992 Oct;12(10):4279–4287. doi: 10.1128/mcb.12.10.4279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Jones A. R., Schedl T. Mutations in gld-1, a female germ cell-specific tumor suppressor gene in Caenorhabditis elegans, affect a conserved domain also found in Src-associated protein Sam68. Genes Dev. 1995 Jun 15;9(12):1491–1504. doi: 10.1101/gad.9.12.1491. [DOI] [PubMed] [Google Scholar]
  30. Kanaar R., Roche S. E., Beall E. L., Green M. R., Rio D. C. The conserved pre-mRNA splicing factor U2AF from Drosophila: requirement for viability. Science. 1993 Oct 22;262(5133):569–573. doi: 10.1126/science.7692602. [DOI] [PubMed] [Google Scholar]
  31. Keller E. B., Noon W. A. Intron splicing: a conserved internal signal in introns of animal pre-mRNAs. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7417–7420. doi: 10.1073/pnas.81.23.7417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Kohtz J. D., Jamison S. F., Will C. L., Zuo P., Lührmann R., Garcia-Blanco M. A., Manley J. L. Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors. Nature. 1994 Mar 10;368(6467):119–124. doi: 10.1038/368119a0. [DOI] [PubMed] [Google Scholar]
  33. Krämer A. Purification of splicing factor SF1, a heat-stable protein that functions in the assembly of a presplicing complex. Mol Cell Biol. 1992 Oct;12(10):4545–4552. doi: 10.1128/mcb.12.10.4545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Krämer A. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu Rev Biochem. 1996;65:367–409. doi: 10.1146/annurev.bi.65.070196.002055. [DOI] [PubMed] [Google Scholar]
  35. Krämer A., Utans U. Three protein factors (SF1, SF3 and U2AF) function in pre-splicing complex formation in addition to snRNPs. EMBO J. 1991 Jun;10(6):1503–1509. doi: 10.1002/j.1460-2075.1991.tb07670.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Kyhse-Andersen J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods. 1984 Dec;10(3-4):203–209. doi: 10.1016/0165-022x(84)90040-x. [DOI] [PubMed] [Google Scholar]
  37. Legrain P., Rosbash M. Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell. 1989 May 19;57(4):573–583. doi: 10.1016/0092-8674(89)90127-x. [DOI] [PubMed] [Google Scholar]
  38. Legrain P., Seraphin B., Rosbash M. Early commitment of yeast pre-mRNA to the spliceosome pathway. Mol Cell Biol. 1988 Sep;8(9):3755–3760. doi: 10.1128/mcb.8.9.3755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. MacMillan A. M., Query C. C., Allerson C. R., Chen S., Verdine G. L., Sharp P. A. Dynamic association of proteins with the pre-mRNA branch region. Genes Dev. 1994 Dec 15;8(24):3008–3020. doi: 10.1101/gad.8.24.3008. [DOI] [PubMed] [Google Scholar]
  40. Madhani H. D., Guthrie C. Dynamic RNA-RNA interactions in the spliceosome. Annu Rev Genet. 1994;28:1–26. doi: 10.1146/annurev.ge.28.120194.000245. [DOI] [PubMed] [Google Scholar]
  41. Michaud S., Reed R. A functional association between the 5' and 3' splice site is established in the earliest prespliceosome complex (E) in mammals. Genes Dev. 1993 Jun;7(6):1008–1020. doi: 10.1101/gad.7.6.1008. [DOI] [PubMed] [Google Scholar]
  42. Michaud S., Reed R. An ATP-independent complex commits pre-mRNA to the mammalian spliceosome assembly pathway. Genes Dev. 1991 Dec;5(12B):2534–2546. doi: 10.1101/gad.5.12b.2534. [DOI] [PubMed] [Google Scholar]
  43. Min H., Turck C. W., Nikolic J. M., Black D. L. A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer. Genes Dev. 1997 Apr 15;11(8):1023–1036. doi: 10.1101/gad.11.8.1023. [DOI] [PubMed] [Google Scholar]
  44. Musco G., Kharrat A., Stier G., Fraternali F., Gibson T. J., Nilges M., Pastore A. The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome. Nat Struct Biol. 1997 Sep;4(9):712–716. doi: 10.1038/nsb0997-712. [DOI] [PubMed] [Google Scholar]
  45. Musco G., Stier G., Joseph C., Castiglione Morelli M. A., Nilges M., Gibson T. J., Pastore A. Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell. 1996 Apr 19;85(2):237–245. doi: 10.1016/s0092-8674(00)81100-9. [DOI] [PubMed] [Google Scholar]
  46. Nandabalan K., Price L., Roeder G. S. Mutations in U1 snRNA bypass the requirement for a cell type-specific RNA splicing factor. Cell. 1993 Apr 23;73(2):407–415. doi: 10.1016/0092-8674(93)90239-m. [DOI] [PubMed] [Google Scholar]
  47. Nandabalan K., Roeder G. S. Binding of a cell-type-specific RNA splicing factor to its target regulatory sequence. Mol Cell Biol. 1995 Apr;15(4):1953–1960. doi: 10.1128/mcb.15.4.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. O'Shea E. K., Klemm J. D., Kim P. S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 1991 Oct 25;254(5031):539–544. doi: 10.1126/science.1948029. [DOI] [PubMed] [Google Scholar]
  49. Oostra B. A., Verkerk A. J. The fragile X syndrome: isolation of the FMR-1 gene and characterization of the fragile X mutation. Chromosoma. 1992 Apr;101(7):381–387. doi: 10.1007/BF00582832. [DOI] [PubMed] [Google Scholar]
  50. Potashkin J., Naik K., Wentz-Hunter K. U2AF homolog required for splicing in vivo. Science. 1993 Oct 22;262(5133):573–575. doi: 10.1126/science.8211184. [DOI] [PubMed] [Google Scholar]
  51. Rain J. C., Legrain P. In vivo commitment to splicing in yeast involves the nucleotide upstream from the branch site conserved sequence and the Mud2 protein. EMBO J. 1997 Apr 1;16(7):1759–1771. doi: 10.1093/emboj/16.7.1759. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Rain J. C., Tartakoff A. M., Krämer A., Legrain P. Essential domains of the PRP21 splicing factor are implicated in the binding to PRP9 and PRP11 proteins and are conserved through evolution. RNA. 1996 Jun;2(6):535–550. [PMC free article] [PubMed] [Google Scholar]
  53. Reed R. Initial splice-site recognition and pairing during pre-mRNA splicing. Curr Opin Genet Dev. 1996 Apr;6(2):215–220. doi: 10.1016/s0959-437x(96)80053-0. [DOI] [PubMed] [Google Scholar]
  54. Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 1994 May;19(1):55–72. doi: 10.1002/prot.340190108. [DOI] [PubMed] [Google Scholar]
  55. Ruby S. W., Abelson J. An early hierarchic role of U1 small nuclear ribonucleoprotein in spliceosome assembly. Science. 1988 Nov 18;242(4881):1028–1035. doi: 10.1126/science.2973660. [DOI] [PubMed] [Google Scholar]
  56. Rymond B. C., Rosbash M. Cleavage of 5' splice site and lariat formation are independent of 3' splice site in yeast mRNA splicing. Nature. 1985 Oct 24;317(6039):735–737. doi: 10.1038/317735a0. [DOI] [PubMed] [Google Scholar]
  57. Scherly D., Dathan N. A., Boelens W., van Venrooij W. J., Mattaj I. W. The U2B'' RNP motif as a site of protein-protein interaction. EMBO J. 1990 Nov;9(11):3675–3681. doi: 10.1002/j.1460-2075.1990.tb07579.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Seraphin B., Rosbash M. Identification of functional U1 snRNA-pre-mRNA complexes committed to spliceosome assembly and splicing. Cell. 1989 Oct 20;59(2):349–358. doi: 10.1016/0092-8674(89)90296-1. [DOI] [PubMed] [Google Scholar]
  59. Siebel C. W., Admon A., Rio D. C. Soma-specific expression and cloning of PSI, a negative regulator of P element pre-mRNA splicing. Genes Dev. 1995 Feb 1;9(3):269–283. doi: 10.1101/gad.9.3.269. [DOI] [PubMed] [Google Scholar]
  60. Siomi H., Choi M., Siomi M. C., Nussbaum R. L., Dreyfuss G. Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome. Cell. 1994 Apr 8;77(1):33–39. doi: 10.1016/0092-8674(94)90232-1. [DOI] [PubMed] [Google Scholar]
  61. Siomi H., Matunis M. J., Michael W. M., Dreyfuss G. The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res. 1993 Mar 11;21(5):1193–1198. doi: 10.1093/nar/21.5.1193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Siomi H., Siomi M. C., Nussbaum R. L., Dreyfuss G. The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell. 1993 Jul 30;74(2):291–298. doi: 10.1016/0092-8674(93)90420-u. [DOI] [PubMed] [Google Scholar]
  63. Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
  64. Sourdive D. J., Transy C., Garbay S., Yaniv M. The bifunctional DCOH protein binds to HNF1 independently of its 4-alpha-carbinolamine dehydratase activity. Nucleic Acids Res. 1997 Apr 15;25(8):1476–1484. doi: 10.1093/nar/25.8.1476. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Staknis D., Reed R. SR proteins promote the first specific recognition of Pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex. Mol Cell Biol. 1994 Nov;14(11):7670–7682. doi: 10.1128/mcb.14.11.7670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Séraphin B., Rosbash M. The yeast branchpoint sequence is not required for the formation of a stable U1 snRNA-pre-mRNA complex and is recognized in the absence of U2 snRNA. EMBO J. 1991 May;10(5):1209–1216. doi: 10.1002/j.1460-2075.1991.tb08062.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Toda T., Iida A., Miwa T., Nakamura Y., Imai T. Isolation and characterization of a novel gene encoding nuclear protein at a locus (D11S636) tightly linked to multiple endocrine neoplasia type 1 (MEN1). Hum Mol Genet. 1994 Mar;3(3):465–470. doi: 10.1093/hmg/3.3.465. [DOI] [PubMed] [Google Scholar]
  68. Transy C., Legrain P. The two-hybrid: an in vivo protein-protein interaction assay. Mol Biol Rep. 1995;21(2):119–127. doi: 10.1007/BF00986502. [DOI] [PubMed] [Google Scholar]
  69. Valcárcel J., Gaur R. K., Singh R., Green M. R. Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA [corrected]. Science. 1996 Sep 20;273(5282):1706–1709. doi: 10.1126/science.273.5282.1706. [DOI] [PubMed] [Google Scholar]
  70. Vernet T., Dignard D., Thomas D. Y. A family of yeast expression vectors containing the phage f1 intergenic region. Gene. 1987;52(2-3):225–233. doi: 10.1016/0378-1119(87)90049-7. [DOI] [PubMed] [Google Scholar]
  71. Wrehlke C., Schmitt-Wrede H. P., Qiao Z., Wunderlich F. Enhanced expression in spleen macrophages of the mouse homolog to the human putative tumor suppressor gene ZFM1. DNA Cell Biol. 1997 Jun;16(6):761–767. doi: 10.1089/dna.1997.16.761. [DOI] [PubMed] [Google Scholar]
  72. Wu J. Y., Maniatis T. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell. 1993 Dec 17;75(6):1061–1070. doi: 10.1016/0092-8674(93)90316-i. [DOI] [PubMed] [Google Scholar]
  73. Xiao S. H., Manley J. L. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev. 1997 Feb 1;11(3):334–344. doi: 10.1101/gad.11.3.334. [DOI] [PubMed] [Google Scholar]
  74. Zamore P. D., Green M. R. Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9243–9247. doi: 10.1073/pnas.86.23.9243. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Zamore P. D., Patton J. G., Green M. R. Cloning and domain structure of the mammalian splicing factor U2AF. Nature. 1992 Feb 13;355(6361):609–614. doi: 10.1038/355609a0. [DOI] [PubMed] [Google Scholar]
  76. Zhang X., Schwer B. Functional and physical interaction between the yeast splicing factors Slu7 and Prp18. Nucleic Acids Res. 1997 Jun 1;25(11):2146–2152. doi: 10.1093/nar/25.11.2146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Zorio D. A., Lea K., Blumenthal T. Cloning of Caenorhabditis U2AF65: an alternatively spliced RNA containing a novel exon. Mol Cell Biol. 1997 Feb;17(2):946–953. doi: 10.1128/mcb.17.2.946. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Zorn A. M., Krieg P. A. The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos. Genes Dev. 1997 Sep 1;11(17):2176–2190. doi: 10.1101/gad.11.17.2176. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from RNA are provided here courtesy of The RNA Society

RESOURCES